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Conserved domains on  [gi|297808381|ref|XP_002872074|]
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uncharacterized protein LOC9308143 [Arabidopsis lyrata subsp. lyrata]

Protein Classification

ML domain-containing protein( domain architecture ID 5313)

ML (MD-2-related lipid-recognition) domain-containing protein; the ML domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi; it is predicted to mediate diverse biological functions through interaction with specific lipids

Gene Ontology:  GO:0008289
PubMed:  12076526

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ML super family cl00274
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
 28-154 1.43e-31

The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi. These single-domain proteins form two anti-parallel beta-pleated sheets stabilized by three disulfide bonds and with an accessible central hydrophobic cavity, and are predicted to mediate diverse biological functions through interaction with specific lipids.


The actual alignment was detected with superfamily member cd00917:

Pssm-ID: 469700  Cd Length: 122  Bit Score: 111.26  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297808381  28 FEYCAKNGNDYGTVTRIEVSPsVGSHGNPTININLFGSASKNISPGTLVYVAFRSGDFTGLLKTYNLCDVST-CNTESEI 106
Cdd:cd00917    1 FEYCDKGGEDIVKVTSVEISP-NPPAAGQNLTIEASGSVGKEIEDGAYVVVEVKYGFIRLLSETYDLCDETKnVDLSCPI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 297808381 107 EAGTNFELTLSDVLyvGFDEEIKYSVSLRQKTleeEDPIIKMCVDFKV 154
Cdd:cd00917   80 EPGDKFLTKLVDLP--GEIPPGKYTVSARAYT---KDDEEITCLSFSV 122
 
Name Accession Description Interval E-value
PG-PI_TP cd00917
The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to ...
 28-154 1.43e-31

The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to bind phosphatidylglycerol and phosphatidylinositol, but the biological significance of this is still obscure. These proteins belong to the ML domain family.


Pssm-ID: 238459  Cd Length: 122  Bit Score: 111.26  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297808381  28 FEYCAKNGNDYGTVTRIEVSPsVGSHGNPTININLFGSASKNISPGTLVYVAFRSGDFTGLLKTYNLCDVST-CNTESEI 106
Cdd:cd00917    1 FEYCDKGGEDIVKVTSVEISP-NPPAAGQNLTIEASGSVGKEIEDGAYVVVEVKYGFIRLLSETYDLCDETKnVDLSCPI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 297808381 107 EAGTNFELTLSDVLyvGFDEEIKYSVSLRQKTleeEDPIIKMCVDFKV 154
Cdd:cd00917   80 EPGDKFLTKLVDLP--GEIPPGKYTVSARAYT---KDDEEITCLSFSV 122
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 25-155 5.76e-17

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 460498  Cd Length: 133  Bit Score: 73.94  E-value: 5.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297808381   25 AIDFEYCAKNGNDYGTVTRIEVSPSVGSHGNPTININLFGSASKNISPGTLVYVAFRSGDFTGLLK---TYNLCDV---- 97
Cdd:pfam02221   1 SVPFRDCGRNKDDAPTPKSVDISPPCPLVRGQNLTISASGTTSDEISQGLKVDVEVRLGGITLPFPlpeTRDLCDElevg 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297808381   98 --STCNTESEIEAGTNFELTLSDVLYVGfdeeiKYSVSLRQKTlEEEDPIikMCVDFKVP 155
Cdd:pfam02221  81 sgLSCPIKAGEYVTYTLTLPLPSEYPPG-----KYTVEAELYD-QDGKPL--TCFKIDVS 132
 
Name Accession Description Interval E-value
PG-PI_TP cd00917
The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to ...
 28-154 1.43e-31

The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to bind phosphatidylglycerol and phosphatidylinositol, but the biological significance of this is still obscure. These proteins belong to the ML domain family.


Pssm-ID: 238459  Cd Length: 122  Bit Score: 111.26  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297808381  28 FEYCAKNGNDYGTVTRIEVSPsVGSHGNPTININLFGSASKNISPGTLVYVAFRSGDFTGLLKTYNLCDVST-CNTESEI 106
Cdd:cd00917    1 FEYCDKGGEDIVKVTSVEISP-NPPAAGQNLTIEASGSVGKEIEDGAYVVVEVKYGFIRLLSETYDLCDETKnVDLSCPI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 297808381 107 EAGTNFELTLSDVLyvGFDEEIKYSVSLRQKTleeEDPIIKMCVDFKV 154
Cdd:cd00917   80 EPGDKFLTKLVDLP--GEIPPGKYTVSARAYT---KDDEEITCLSFSV 122
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 25-155 5.76e-17

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 460498  Cd Length: 133  Bit Score: 73.94  E-value: 5.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297808381   25 AIDFEYCAKNGNDYGTVTRIEVSPSVGSHGNPTININLFGSASKNISPGTLVYVAFRSGDFTGLLK---TYNLCDV---- 97
Cdd:pfam02221   1 SVPFRDCGRNKDDAPTPKSVDISPPCPLVRGQNLTISASGTTSDEISQGLKVDVEVRLGGITLPFPlpeTRDLCDElevg 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 297808381   98 --STCNTESEIEAGTNFELTLSDVLYVGfdeeiKYSVSLRQKTlEEEDPIikMCVDFKVP 155
Cdd:pfam02221  81 sgLSCPIKAGEYVTYTLTLPLPSEYPPG-----KYTVEAELYD-QDGKPL--TCFKIDVS 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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